5FBG
S1 nuclease from Aspergillus oryzae, mutant D65N, in complex with phosphate, 2'-deoxycytidine and 2'-deoxyguanosine.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003676 | molecular_function | nucleic acid binding |
| A | 0004518 | molecular_function | nuclease activity |
| A | 0004519 | molecular_function | endonuclease activity |
| A | 0005575 | cellular_component | cellular_component |
| A | 0006308 | biological_process | DNA catabolic process |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016788 | molecular_function | hydrolase activity, acting on ester bonds |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0003676 | molecular_function | nucleic acid binding |
| B | 0004518 | molecular_function | nuclease activity |
| B | 0004519 | molecular_function | endonuclease activity |
| B | 0005575 | cellular_component | cellular_component |
| B | 0006308 | biological_process | DNA catabolic process |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0016788 | molecular_function | hydrolase activity, acting on ester bonds |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PROSITE/UniProt
| site_id | PS00136 |
| Number of Residues | 12 |
| Details | SUBTILASE_ASP Serine proteases, subtilase family, aspartic acid active site. STVLDDGLayiN |
| Chain | Residue | Details |
| A | SER237-ASN248 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 16 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:28036383, ECO:0007744|PDB:5FB9, ECO:0007744|PDB:5FBA, ECO:0007744|PDB:5FBB, ECO:0007744|PDB:5FBC, ECO:0007744|PDB:5FBD, ECO:0007744|PDB:5FBF, ECO:0007744|PDB:5FBG |
| Chain | Residue | Details |
| A | TRP21 | |
| B | HIS26 | |
| B | HIS80 | |
| B | HIS135 | |
| B | ASP139 | |
| B | HIS145 | |
| B | HIS168 | |
| B | ASP172 | |
| A | HIS26 | |
| A | HIS80 | |
| A | HIS135 | |
| A | ASP139 | |
| A | HIS145 | |
| A | HIS168 | |
| A | ASP172 | |
| B | TRP21 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:28036383, ECO:0007744|PDB:5FBD, ECO:0007744|PDB:5FBF |
| Chain | Residue | Details |
| A | ASN65 | |
| B | ASN65 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:P24289 |
| Chain | Residue | Details |
| A | GLY93 | |
| B | GLY93 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | SITE: Important for catalytic activity => ECO:0000269|PubMed:28036383 |
| Chain | Residue | Details |
| A | ASN65 | |
| B | ASN65 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | SITE: Important for catalytic activity => ECO:0000250|UniProtKB:P24289 |
| Chain | Residue | Details |
| A | LYS68 | |
| B | LYS68 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498, ECO:0000269|PubMed:28036383, ECO:0007744|PDB:5FB9, ECO:0007744|PDB:5FBB, ECO:0007744|PDB:5FBC, ECO:0007744|PDB:5FBD, ECO:0007744|PDB:5FBF, ECO:0007744|PDB:5FBG |
| Chain | Residue | Details |
| A | ASN112 | |
| B | ASN112 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498 |
| Chain | Residue | Details |
| A | ASN122 | |
| B | ASN122 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498, ECO:0000269|PubMed:28036383, ECO:0007744|PDB:5FB9, ECO:0007744|PDB:5FBA, ECO:0007744|PDB:5FBB, ECO:0007744|PDB:5FBC, ECO:0007744|PDB:5FBF, ECO:0007744|PDB:5FBG |
| Chain | Residue | Details |
| A | ASN248 | |
| B | ASN248 |
